Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease ( IF 4.2 ) Pub Date : 2021-06-16 , DOI: 10.1016/j.bbadis.2021.166202 Surbhi Chaudhary 1 , Asmita Dhiman 1 , Anil Patidar 1 , Himanshu Malhotra 1 , Sharmila Talukdar 1 , Rahul Dilawari 1 , Gaurav Kumar Chaubey 1 , Radheshyam Modanwal 1 , Chaaya Iyengar Raje 2 , Manoj Raje 1
Onset of protein aggregation reflects failure of the cellular folding machinery to keep aggregation-prone protein from misfolding and accumulating into a non-degradable state. FRET based analysis and biochemical data reveal that cytosolic prion (cyPrP) and httQ-103 interact with the multifunctional protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) leading to few detectable aggregates in GAPDH-over expressing cells.The preventive effect of GAPDH suggests that this abundant and long-lived cytoplasmic protein has an active role in the shielding and maintenance, in soluble form of proteins as heterogeneous as huntingtin and cyPrP.
中文翻译:
Moonlighting 3-磷酸甘油醛脱氢酶(GAPDH)调节蛋白质聚集
蛋白质聚集的开始反映了细胞折叠机制未能防止易于聚集的蛋白质错误折叠并积累成不可降解状态。基于 FRET 的分析和生化数据显示,胞质朊病毒 (cyPrP) 和 httQ-103 与多功能蛋白 3-磷酸甘油醛脱氢酶 (GAPDH) 相互作用,导致 GAPDH 过表达细胞中几乎没有可检测的聚集体。 GAPDH 的预防作用表明这种丰富且寿命长的细胞质蛋白在保护和维持蛋白质的可溶性形式中具有积极作用,如亨廷顿蛋白和 cyPrP 等异质蛋白。